Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Application Status
This action is written in response to applicant’s correspondence received 02/13/2026. Claims 25, 28-37, and 39-45 are currently pending. Claim 43 is withdrawn from prosecution as being drawn to non-elected subject matter. Accordingly, claims 25, 28-37, 39-42 and 44-45 are examined herein.
Any rejection or objection not reiterated herein has been overcome by amendment. Applicant' s amendments and arguments have been thoroughly reviewed, but are not persuasive to place the claims in condition for allowance for the reasons that follow.
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 40 and 41 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claims 40 and 41, as amended, recite the limitation "the cohesin domain". There is insufficient antecedent basis for this limitation in the claim. Claim 40 has been amended to depend from claim 25 instead of claim 29. Claim 41, which also depends from claim 25, has been amended to change the term “a cohesin domain” to “the cohesin domain”. However, claim 25 does not recite a cohesin domain.
Amending the rejected claims to recite “a cohesin domain”, or amending claim 25 to, e.g., incorporate the limitations of claim 29, which recites a cohesin domain, would obviate this rejection.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 25, 30, 36. 37, 39 and 42 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Gao (Gao et al. Hepatocyte-targeted HFE and TFR2 control hepcidin expression in mice. Blood (2010) 115 (16): 3374–3381.), as evidenced by Kawabata (Kawabata et al. Molecular Cloning of Transferrin Receptor 2: A NEW MEMBER OF THE TRANSFERRIN RECEPTOR-LIKE FAMILY. Journal of Biological Chemistry, Volume 274, Issue 30, 1999, Pages 20826-20832.).
Please note: Claim 25 has been amended to generically recite a ligand-binding domain instead of the previously recited and narrower limitation of a ligand-binding domain of a non-mammalian protein. As a result, the broadest reasonable interpretation of amended claim 25 now encompasses canonical transferrin or nerve growth factor receptors and sequences encoding them, because those receptors, by themselves, meet the recited structural requirements of a transferrin or NGF receptor comprising a ligand-binding domain and at least one of a intracellular, transmembrane, and/or extracellular domain.
Regarding claim 25, Gao teaches, “recombinant adeno-associated virus, AAV2/8, for hepatocyte-specific expression of…Tfr2 in mice”, speaking of transferrin-receptor 2 (Abstract). As evidenced by Kawabata (which Gao cites), Tfr2 is a transmembrane receptor comprising an intracellular domain, a transmembrane domain, and a ligand-binding extracellular domain (please see FIG. 1A, specifically the map of isoform TfR2-α).
Gao further teaches that the vector carried a hepatic-specific promoter (p. 3375):
…we used a recombinant serotype 2 adeno associated virus vector pseudotyped with serotype 8 capsid (AAV2/8) and carrying a hepatic-specific promoter to express either Hfe or Tfr2 in mice…
Regarding claim 30, Gao teaches that the promoter sequence is a tissue-specific promoter sequence (i.e., hepatic specific; see above).
Regarding claims 36 and 37, Gao teaches that the nucleic acid further comprises an enhancer sequence, i.e. one or more additional sequences that facilitate expression of the receptor:
…liver-specific promoter (LSP) in a plasmid containing AAV serotype 2 inverted terminal repeats. The LSP contains promoter sequences from the thyroid hormone-binding globulin gene (~382 to 3) and 2 copies of the α1-microglobulin/bikunin enhancer sequence (~2804 to ~2704).38 Tfr2 was amplified from mouse liver cDNA and inserted into the same AAV2 vector plasmid
Regarding claim 39, Gao teaches wherein the nucleic acid comprises ITR sequences derived from AAV2 (see above).
Regarding claim 42, insofar in Gao teaches that the AAVs were administered to mice in vivo, Gao teaches that the AAVs were comprised within a pharmaceutical composition, i.e., a composition suitable for in vivo administration.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
Determining the scope and contents of the prior art.
Ascertaining the differences between the prior art and the claims at issue.
Resolving the level of ordinary skill in the pertinent art.
Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 25, 28, 29, 30-31, 34-37, 39, 41-42 and 44 are rejected under 35 U.S.C. 103 as being unpatentable over U.S. Patent Publication No. 2005/0106700 A1 to Nomura (of record, hereinafter ‘Nomura’) in view of U.S. Patent No. 8,865,881 to Balazs (hereinafter ‘Balazs’) and Martin & Uprichard (Proc. Natl. Acad. Sci. U.S.A. (2013). 110 (26) 10777-10782).
Regarding claims 25, 41 and 44, Nomura teaches a method of purifying a recombinant fused protein, the method comprising use of an expression vector comprising a nucleic acid containing a promoter sequence and a sequence that encodes any recombinant protein having a ligand-binding domain of a non-mammalian (bacterial; C. josui) protein (dockerin):
A method of purifying a recombinant fused protein characterized in that a recombinant fused protein, wherein a target protein has been fused with dockerin by genetic engineering techniques, is treated with a support having a cohesin domain immobilized thereon; and a method of producing a target protein characterized by comprising obtaining a recombinant fused protein having the target protein bound to dockerin with the use of an expression vector having a gene encoding the target protein and the dockerin inserted thereinto (abstract)
[0105] The dockerin genes used for constructing the above-mentioned expression vector include, for example, a gene cloned by a conventional method, which is from a cellulase complex derived from C. josui…There is no particular restriction on the target protein genes, and therefore a gene encoding various known proteins may be used.
[0104] More specifically, the recombinant fused protein can be obtained by inserting a dockerin gene as an affinity peptide into the 5'-upstream region or the 3'-downstream region of a target protein gene, which is inserted into the downstream of the promoter of a given expression vector, thereby constructing an expression vector for producing the recombinant fused protein of the dockerin and the given protein, and then by introducing the expression vector into a host to produce the protein.
Nomura teaches that the recombinant fused protein can be separated and purified with the use of specific binding of dockerin and cohesion regardless of the properties of target proteins [para 0347].
Nomura does not teach wherein the expression vector is an rAAV particle. Nomura also does not teach wherein the non-mammalian ligand-binding domain is fused to at least one domain of a transferrin receptor or a nerve growth factor receptor.
Balazs teaches a recombinant AAV which, “can be used to produce a protein of interest in vitro, for example, in a cell culture.” (col 26 ln 14-16). Balazs further teaches that the proteins produced by the AAV can be useful in applications such as research, compound screening, and drug discovery (col 26 ln 10-12), that the AAV allows for high production of the proteins of interest (col 25 ln 21-22), and that protein of interest is not in any way limited (col 26 ln 31-32). Lastly, Balazs indicates that the protein of interest can be isolated in accordance with conventional methods known in the art (col 20 ln 32-40).
Neither Nomura nor Balazs teach a protein comprising the non-mammalian ligand binding domain and a transferrin or nerve growth factor receptor.
Martin & Uprichard provide a teaching, suggestion or motivation to study the role of the transferrin receptor 1 (TfR1) in hepatitis C virus (HCV) infection, including binding interactions between TfR1 and the HCV virion:
we found that TfR1 mediates HCV entry (§Abstract)
Our data suggest that TfR1 binds the HCV virion and may contribute specifically to virion endocytosis... As such, more extensive studies on the role of TfR1 in HCV entry may contribute to better understanding of the mechanisms involved in virion internalization (p. 10781 §Interplay Between Iron Homeostasis and HCV Infection)
It would have been prima facie obvious to a person having ordinary skill in the art before the effective filing date of the claimed invention to have combined the expression vector and method of purifying a recombinant protein using the cohesion/dockerin tag system, as taught by Nomura, with the AAV for in vitro protein production as taught by Balazs. The skilled artisan would have been motivated to combine the AAV vector as taught by Balazs based on their teachings that the vector yielded high protein expression for in vitro production. The skilled artisan would have been further motivated by Martin & Uprichard’s teachings regarding the role of TfR1 in HCV to apply those combined, general tools for protein production and purification to TfR1 specifically, to research the role of TfR1 in HCV infection, for example by conducting studies to determine how HCV proteins and TfR1 interact with each other.
Regarding claims 28, 29 and 31, it is relevant to note that while Nomura teaches the bacterial dockerin domain fused to the protein, and the instant claims recite the bacterial cohesin domain fused to the instant protein, Nomura makes clear that the purification system relies on the interaction between dockerin and cohesin. As described by Nomura, the function of the dockerin/cohesin system was known in the art. One having ordinary skill in the art could have substituted the dockerin domain of Nomura with its corresponding cohesin domain, and the result would have predictably led to an affinity purification system based on the cohesin/dockerin protein and ligand pair.
Regarding claim 30, Balazs teaches wherein the promoter is a tissue-specific promoter (regulatory element):
Typically, gene expression is placed under the control of one or more regulatory elements, for example, without limitation, constitutive or inducible promoters, tissue-specific regulatory elements, and enhancers. (col 10 ln 11-14)
To evaluate the expression potential of various promoters in muscle expression, a series of vectors carrying the luciferase gene driven by a panel of ubiquitous and tissue-specific promoters were made.(col 36 ln 37-40)
Regarding claim 34, Balazs teaches wherein the promoter sequence is a hybrid CMV-B actin promoter sequence (col 13 ln 47-50):
Examples of viral promoters include…CAG promoter (which is a combination of the CMV early enhancer element and chicken beta-actin promoter
Regarding claim 35, Balazs teaches that, “It is contemplated by the present application that the cap genes and/or rep gene from any AAV serotype (including, but not limited to, AAV1, AAV2, AAV4, AAV5, AAV6, AAV7, AAV8, AAV9, and any variants thereof) can be used herein to produce the recombinant AAV disclosed herein to express one or more proteins of interest.” (col 25 ln 6-13).
Regarding claims 36-37, Balazs teaches that the nucleic acid further comprises one or more additional sequences that facilitate expression of the protein and are operatively linked to its coding sequence, such as termination signals, poly(A) tails, etc.:
the viral posttranscriptional regulatory element is woodchuck hepatitis virus posttranscriptional regulatory element (WPRE), hepatitis B virus posttranscriptional regulatory element (HBVPRE), RNA transport element (RTE), or any variant thereof. (col 3 ln 14-17)
the viral vector further comprises a transcription termination region downstream of the posttranscriptional regulatory element. In some embodiments, the
transcription termination region comprises an SV40 late poly (A) sequence, a rabbit beta-globin poly(A) sequence, a bovine growth hormone poly(A) sequence, or any variant thereof. (col 3 ln 19-25)
Regarding claim 39, Balazs teaches that the nucleic acid comprises ITR sequences derived from AAV1/2/4 or 9:
AAV sequences begin immediately following the XhoI restriction site with a 145bp “flip'-inverted terminal repeat (ITR) from AAV2…a second 145bp AAV2 "flop”-ITR (col 37 ln 11-12, 23)
Regarding claim 42, Nomura provides a teaching, suggestion or motivation to use the recombinant protein to study pharmacokinetics in cells and tissues:
[0127] Conventionally, in order to detect and quantify a target protein, an antibody against the target protein has to be prepared for each protein. If a recombinant fused protein containing dockerin and a target protein is used, the target protein can be detected and quantified easily with a labeled cohesin domain.
[0128] Furthermore, detection and quantification of a recombinant fused protein wherein a target protein has been fused with dockerin with a labeled cohesin domain according to the above-mentioned method will enable to measure or detect the expression amount of the target protein and localization or pharmacokinetics in the cells and tissues.
Therefore, it would also have been obvious to have make a composition comprising the AAV and a pharmaceutical carrier to study the pharmacokinetics of the recombinant protein fused with dockerin/cohesin.
Claims 40 and 45 are rejected under 35 U.S.C. 103 as being unpatentable over U.S. Patent Publication No. 2005/0106700 A1 to Nomura (of record, hereinafter ‘Nomura’) in view of U.S. Patent No. 8,865,881 to Balazs (hereinafter ‘Balazs’) and Martin & Uprichard (Proc. Natl. Acad. Sci. U.S.A. 110 (26) 10777-10782), as applied to claims 25, 28, 29, 30-31, 34-37, 39, 41-42 and 44, further in view of Craig (Craig et al. Journal of Biotechnology, Volume 121, Issue 2, 2006, Pages 165-173.).
Nomura, Balazs and Martin & Uprichard render obvious the invention of claims 25 and 29, from which claim 40 depends.
Nomura, Balazs and Martin & Uprichard also render obvious a rAAV comprising a nucleic acid containing a promoter sequence that encodes a receptor comprising a non-mammalian cohesin domain, as discussed above.
Nomura, Balazs and Martin & Uprichard do not teach wherein the cohesin domain is a cohesin 7 domain.
Craig teaches a dockerin/cohesin system using cohesin 7 (Cip7) and dockerin (Doc) domains of Clostridium thermocellum for affinity purification of proteins (Abstract).
It would have been prima facie obvious to a person having ordinary skill in the art before the effective filing date of the claimed invention to have substituted the cohesin domain in Nomura’s affinity purification system, combined with Balazs protein production system using rAAVs, with the cohesion 7 domain taught by Craig. The prior art taught methods and products which differ from the claimed product by the substitution of a cohesin domain. The substituted component, cohesin 7, was known in the art and was used in a highly analogous protein purification system. One of ordinary skill in the art could have substituted one cohesin domain for another, and the results of the substitution would have predictably yielded a functional cohesin/dockerin affinity purification system.
Claims 32-33 are rejected under 35 U.S.C. 103 as being unpatentable over U.S. Patent Publication No. 2005/0106700 A1 to Nomura (of record, hereinafter ‘Nomura’) in view of U.S. Patent No. 8,865,881 to Balazs (hereinafter ‘Balazs’) and Martin & Uprichard (Proc. Natl. Acad. Sci. U.S.A. 110 (26) 10777-10782), as applied to claims 25, 28, 29, 30-31, 34-37, 39, 41-42 and 44, further in view of Kleine & Benes (Cytometry, 69A: 147-151. 2006.) and Bien-Ly (Transferrin receptor (TfR) trafficking determines brain uptake of TfR antibody affinity variants. J Exp Med (2014) 211 (2): 233–244.)
Nomura, Balazs and Martin & Uprichard render obvious the invention of claims 25 and 30, from which claims 32-33 depend.
Nomura, Balazs and Martin & Uprichard do not teach wherein the promoter sequence is ICAM-2.
Kleine & Benes teach that cell adhesion molecules (CAM) are involved in lymphocyte transfer through the blood brain barrier and blood-cerebrospinal fluid (abstract). Kleine and Benes also teach that ICAM-2 is expressed on human brain endothelium (Table 1).
Bien-Ly teach that the transferrin receptor is highly expressed on brain endothelial cells (p. 233). Bien-Ly further provides a teaching, suggestion or motivation to detect the expression and localization of the transferrin receptor by noting that the precise cellular mechanisms associated with TfR trafficking at the BBB remains unclear (p. 233).
It would have been prima facie obvious to a person having ordinary skill in the art before the effective filing date of the claimed invention to have combined the rAAV as taught by Nomura, Balazs and Martin & Uprichard with the teachings of Kleine & Benes and Bien-Ly to obtain an rAAV comprising a recombinant transferrin receptor with a cohesin domain and a detectable label under the control of an ICAM-2 promoter. The skilled artisan would have been motivated by the combined teachings of Kleine & Benes and Bien-Ly, which provide a reason to measure transferrin localization and expression by expressing a recombinant, labeled transferrin, as taught by Bien-Ly, along with a suitable promoter for expression transferrin in cells of the BBB, as taught by Kleine & Benes.
Claims 25, 28, 29, 30-31, 34-37, 39, 41-42 and 44 are rejected under 35 U.S.C. 103 as being unpatentable over U.S. Patent Publication No. 2005/0106700 A1 to Nomura (of record, hereinafter ‘Nomura’) in view of U.S. Patent No. 8,865,881 to Balazs (hereinafter ‘Balazs’) and Martin & Uprichard, further in view of Massa (Massa et al. Journal of Neuroscience 17 May 2006, 26 (20) 5288-5300.).
Nomura, Balazs and Martin & Uprichard render obvious the limitations of the claims insofar as they relate to the use of Nomura’s cohesin/dockerin purification system and Balazs’s recombinant AAV for protein production of a transferrin receptor fused to a non-mammalian protein, as discussed above.
Nomura, Balazs and Martin & Uprichard do not teach application of those combined systems to the production of a nerve growth factor receptor.
Massa provides a teaching, suggestion or motivation to apply those general systems to screening for small molecule ligands of p75NTR, a nerve growth factor receptor. Massa notes that, “small molecule p75NTR ligands that positively regulate survival might be found. A pharmacophore designed to capture selected structural and physical chemical features of a neurotrophin domain known to interact with p75NTR was applied to in silico screening of small molecule libraries. Small, nonpeptide, monomeric compounds were identified that interact with p75NTR. In cells showing trophic responses to neurotrophins, the compounds promoted survival signaling through p75NTR-dependent mechanisms. In cells susceptible to proneurotrophin-induced death, compounds did not induce apoptosis but inhibited proneurotrophin-mediated death. These studies identify a unique range of p75NTR behaviors that can result from isolated receptor liganding and establish several novel therapeutic leads.” (Abstract).
It would have been prima facie obvious to a person having ordinary skill in the art before the effective filing date of the claimed invention to have combined the expression vector and method of purifying a recombinant protein using the coheson/dockerin tag system, as taught by Nomura and Balazs, with the nerve growth factor receptor as taught by Massa, to produce and purify P75NTR for in vitro screening of small molecule ligands with potential therapeutic relevance. The skilled artisan would have been motivated to do so by Massa’s teaching that in silico screening for small molecule ligands of P75NTR identified several therapeutic leads suitable for further in vitro investigation.
Response to Arguments
Applicant's arguments filed 02/13/2026 have been fully considered but they are not persuasive for the reasons that follow.
On page 6 of the remarks, Applicant argues, “There is no motivation to reformulate the dockerin-target protein complex described in Nomura as an rAAV vector as described in Balazs because the purpose of Nomura's method is not to deliver a therapeutic payload in vivo, but instead to obtain the target protein from the dockerin-target protein complex in vitro..” Respectfully, this argument is not convincing because, as described above, the teachings cited from Balazs concern a recombinant AAV which, “can be used to produce a protein of interest in vitro, for example, in a cell culture.” (col 26 ln 14-16), and that the AAV allows for high production of the proteins of interest (col 25 ln 21-22). As Balazs notes, the protein can then be isolated in accordance with conventional methods known in the art (col 20 ln 32-40), such as via Nomura’s cohesin/dockerin tag system. Applicant further notes that, “Balazs provides examples of proteins of interest, including hundreds of proteins ranging from antibodies to luciferases (see col. 16-19); however, ligand-binding domains, the transferrin receptor, and the nerve growth factor receptor are not mentioned.” Respectfully, in response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). In the instant case, Balazs and Nomura in combination provide systems for the expression of any proteins of interest in cell culture and their subsequent purification, respectively, while Martin provides a motivation to purify the transferrin receptor in particular for study by teaching that TfR1 is a protein of interest in HCV infection, and that further study of its interactions with HCV should be performed. Applicant’s argument that, “Martin does not teach that TfR1 could be used as a therapeutic agent, but rather that it has a role in HCV entry” is unpersuasive because, as discussed in the above rejections, the combination of references does not lead to a therapeutic agent, but rather to an expression vector encoding tagged TfR1 for in vitro purification.
Applicant also notes that, “the claimed rAAV particles can surprisingly facilitate movement of therapeutic molecules across the BCSFB and delivery of therapeutic agents to the choroid plexus”. While this is acknowledged, the argument is not persuasive because it concerns a particular use for the claimed structure. Per MPEP 2144.IV, “The reason or motivation to modify the reference may often suggest what the inventor has done, but for a different purpose or to solve a different problem. It is not necessary that the prior art suggest the combination to achieve the same advantage or result discovered by applicant”.
Lastly, in response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971).
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to AMANDA M ZAHORIK whose telephone number is (703)756-1433. The examiner can normally be reached M-F 8:00-16:00 EST.
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/A.M.Z./Examiner, Art Unit 1636
/BRIAN WHITEMAN/Primary Examiner, Art Unit 1636
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